Collagen IV α2 (Cleaved-Ser1485) rabbit pAb

• Background :

  Domain:Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain., function:Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Potently inhibits angiogenesis and tumor growth., PTM:Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains., PTM:The trimeric structure of the NC1 domains may be stabilized by covalent bonds between Lys and Met residues., PTM:Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens., similarity:Belongs to the type IV collagen family., similarity:Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain., subunit:There are six type IV collagen isoforms, alpha 1 (IV) -alpha 6 (IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

• Description :

  Domain: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. function: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Potently inhibits angiogenesis and tumor growth. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. PTM: The trimeric structure of the NC1 domains may be stabilized by covalent bonds between Lys and Met residues. PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. similarity: Belongs to the type IV collagen family. similarity: Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain. subunit: There are six type IV collagen isoforms, alpha 1 (IV)-alpha 6 (IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

• UniProt :

  P08572

• Swiss Prot :

  P08572

• Reactivity :

  Human; Mouse

• Immunogen :

  Synthesized peptide derived from human Collagen IV α2 (Cleaved-Ser1485)

• Clonality :

  Polyclonal

• Source :

  Rabbit

• Applications :

  WB; ELISA

• Concentration :

  1 mg/ml

• Dilution :

  WB 1:1000-2000 ELISA 1:5000-20000

• Molecular Weight :

  160 190kD

• Storage Conditions :

  -20°C/1 year

• Observed Molecular Weight :

  160 190kD

• Fragment :

  IgG

• Subcellular Location :

  Secreted, extracellular space, extracellular matrix, basement membrane.

• Other Product Names :

  Collagen alpha-2 (IV) chain [Cleaved into: Canstatin]

• Gene ID (Human) :

  1284